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3MO8

PWWP Domain of Human Bromodomain and PHD finger-containing protein 1 In Complex with Trimethylated H3K36 Peptide

Summary for 3MO8
Entry DOI10.2210/pdb3mo8/pdb
Related3L42
DescriptorPeregrin, Histone H3.2 TRIMETHYLATED H3K36 PEPTIDE (3 entities in total)
Functional Keywordsperegrin, protein br140, histone h3 acetylation, transcription, structural genomics consortium, sgc
Biological sourceHomo sapiens (human)
More
Cellular locationNucleus : P55201 Q71DI3
Total number of polymer chains2
Total formula weight16433.07
Authors
Lam, R.,Zeng, H.,Ni, S.,Bountra, C.,Weigelt, J.,Arrowsmith, C.H.,Edwards, A.M.,Bochkarev, A.,Min, J.,Wu, H.,Structural Genomics Consortium (SGC) (deposition date: 2010-04-22, release date: 2010-06-02, Last modification date: 2023-09-06)
Primary citationWu, H.,Zeng, H.,Lam, R.,Tempel, W.,Amaya, M.F.,Xu, C.,Dombrovski, L.,Qiu, W.,Wang, Y.,Min, J.
Structural and Histone Binding Ability Characterizations of Human PWWP Domains.
Plos One, 6:e18919-e18919, 2011
Cited by
PubMed Abstract: The PWWP domain was first identified as a structural motif of 100-130 amino acids in the WHSC1 protein and predicted to be a protein-protein interaction domain. It belongs to the Tudor domain 'Royal Family', which consists of Tudor, chromodomain, MBT and PWWP domains. While Tudor, chromodomain and MBT domains have long been known to bind methylated histones, PWWP was shown to exhibit histone binding ability only until recently.
PubMed: 21720545
DOI: 10.1371/journal.pone.0018919
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.69 Å)
Structure validation

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